50439-35-5

Basic information

• Product Name: BOC-ALA-ALA-PNA
• Synonyms: N-BOC-L-ALA-ALA-P-NITROANILIDE;BOC-L-ALANYL-ALANINE P-NITROANILIDE;BOC-ALA-ALA-PNA;BOC-ALA-ALA-P-NITROANILIDE;N-T-BOC-ALA-ALA P-NITROANILIDE);N-(tert-butoxycarbonylmethyl)alanine-alanine-nitroanilide
• CAS NO: 50439-35-5
• Molecular Formula: C₁₇H₂₄N₄O₆
• Molecular Weight: 380.4
• Mol File: 50439-35-5.mol
• Article Data: 8

Chemical Properties

• Boiling Point: 654.8±50.0 °C(Predicted)
• Appearance: /
• Density: 1.259±0.06 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 11.34±0.46(Predicted)
• CAS DataBase Reference: BOC-ALA-ALA-PNA(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-ALA-ALA-PNA(50439-35-5)
• EPA Substance Registry System: BOC-ALA-ALA-PNA(50439-35-5)

Safety Data

• Hazardous Substances Data: 50439-35-5(Hazardous Substances Data)

Usage

General Description

BOC-ALA-ALA-PNA is a chemical compound used in peptide synthesis and related biochemical research. It is a derivative of the amino acid alanine and contains a protective BOC (tert-butyloxycarbonyl) group to prevent unwanted reactions during the synthesis process. The compound also contains a PNA (peptide nucleic acid) moiety, making it useful in the development of peptide nucleic acid-based diagnostics and therapeutics. BOC-ALA-ALA-PNA is often used as a building block in the assembly of peptides and peptidomimetics for various research applications, including drug discovery, biochemical studies, and materials science.

Upstream product

• 15761-38-3 L-N-Boc-Ala 
• 1668-13-9 L-alanine-p-nitroanilide 
• 181117-99-7 tert-butyloxycarbonylalanine 4-guanidinophenyl ester 
• 221017-30-7 C₃₅H₃₆N₄O₈ 
• 221017-26-1 C₃₅H₃₆N₄O₈ 
• 221017-34-1 C₃₅H₃₆N₄O₈ 
• 221017-22-7 C₃₅H₃₆N₄O₈ 
• 1026750-87-7 C₃₂H₃₆N₄O₈ 

Downstream Products

• 223753-63-7 Boc-Val-ψ-(CH2-NH)-Ala-Ala-pNA 

Relevant articles and documents

Application of various inverse substrates to thrombin-catalyzed peptide synthesis

Thrombin-catalyzed peptide synthesis has been studied using nine series of 'inverse substrates' i.e., pamidinophenyl, p- and m-guanidinophenyl, p- and m-(guanidinomethyl)phenyl, and four position isomers of guanidinonaphthyl esters derived from N(α)-(tert

Trypsin-catalyzed synthesis of dipeptide containing α-aminoisobutylic acid using p- and m-(amidinomethyl)phenyl esters as acyl donor

Two series of inverse substrates, p- and m-(amidinomethyl)phenyl esters derived from N-(tert-butyloxycarbonyl) amino acid, were prepared as acyl donor components for enzymatic peptide synthesis. They were found to be readily coupled with an acyl acceptor such as L-alanine p-nitroanilide to produce dipeptide. An α-aminoisobutyric acid containing dipeptide was especially obtained in satisfactory yield. Streptomyces griseus trypsin was a more efficient catalyst than the bovine trypsin. The optimum condition for the coupling reaction was studied by changing the organic solvent, pH, and acyl acceptor concentration. It was found that the enzymatic hydrolysis of the resulting product was negligible.

Enzymatic peptide synthesis with p-guanidinophenyl and p- (guanidinomethyl)phenyl esters as acyl donors

Two series of 'inverse substrates', N-Boc-amino acid p-guanidinophenyl and p-(guanidinomethyl)phenyl esters, were prepared as acyl donor components for enzymatic peptide synthesis. The kinetic behavior of these esters toward bovine and Streptomyces griseus (SG) trypsin was analyzed. The spatial requirement of the active site of these enzymes for catalytic efficiency is discussed based on the steric characteristics of the substrates. These substrates were found to couple readily with amino acid p-nitroanilides to produce peptides. SG trypsin was the most efficient catalyst among the enzymes tested (bovine, porcine, and SG trypsin).